Technical Data
Spectrin, alpha (Spectrin Non-erythroid alpha Chain, Alpha Fodrin, Alpha II Spectrin, FLJ44613, Spectrin alpha Non-erythrocytic 1, SPTAN1, SPTA2)
Fodrin (also named nonerythroid spectrin) is a universally expressed membrane-associated cytoskeletal protein consisting of alpha-and beta-subunits (1). This protein is important for maintaining normal membrane structure and supporting cell surface protein function (1). Alpha-fodrin is one of the primary targets cleaved by caspases during apoptosis. The full length 240kD protein can be cleaved at several sites within its sequence by activated caspases, to yield Nterminal 150kD, C-terminal 120kD and 35kD major products (25). Cleavage of alpha-fodrin leads to membrane malfunction and cell shrinkage.

Suitable for use in Western Blot and ELISA. Other applications not tested.

Recommended Dilution:
Western Blot: 1:1000
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage, store at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
PabIgGAffinity Purified
100ul4C (-20C Glycerol)Blue IceHumanRabbit
Not determined
Synthetic peptide corresponding to residues surrounding Asp1185 of human alpha-fodrin (KLH).
Purified by Protein A affinity chromatography.
Supplied as liquid in 10mM HEPES, pH 7.5, 150mM sodium chloride, 0.1mg/ml BSA, 50% glycerol. No preservative added.
Recognizes total levels of human endogenous full length alphafodrin (240kD) and its large fragment (150kD) following cleavage by caspase(s) at Asp1185.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Bennett, B. and Gilligan, D.M. (1993) Annu. Rev. Cell Biol. 9, 2766. 2. Vanags, D.M. et al. (1996) J. Biol. Chem. 271, 3107531085. 3. Cryns, V.L. et al. (1996) J. Biol. Chem. 271, 3127731282.
4. Wang, K.K. et al. (1998) J. Biol. Chem. 273, 2249022497. 5. Janicke, R.U. et al. (1998) J. Biol. Chem. 273, 1554015545.